Temperature Sensitivity and Pressure Resistance of Mushroom Polyphenoloxidase

Authors

  • C. WEEMAES,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • P. RUBENS,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • S. De CORDT,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • L. LUDIKHUYZE,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • I. VAN DEN BROECK,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • M. HENDRICKX,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • K. HEREMANS,

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • P. TOBBACK

    1. Authors Weemaes, De Cordt, Ludikhuyze, Van den Broeck, Hendrickx, and Tobback are with the Dept. of Food & Microbial Technology, Faculty of Agricultural & Applied Biological Sciences, Katholieke Universiteit Leuven, Kardinaal Mercierlaan 92, B-3001 Leuven, Belgium. Authors Rubens and Heremans are with the Dept. of Chemistry, Katholieke Universiteit Leuven, Celestijnenlaan 200D, B-3001 Leuven, Belgium. Direct inquiries to Prof. M. Hendrickx.
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  • This research has been supported by the Flemish Institute for the promotion of scientifictechnological research in industry (IWT), KULeuven Research Council (project OT/94/19) and National Fund for Scientific Research (project G.0189.95).

ABSTRACT

Measurements of residual enzyme activity and FTIR-spectroscopy revealed that mushroom polyphenoloxidase is a thermosensitive enzyme readily inactivated by temperatures exceeding 50°C. The enzyme is, however, very pressure stable. At room temperature no enzyme inactivation occurred at pressures up to 6 kbar. FTIR-spectroscopy revealed that a modification in enzyme conformation occurred below 9 kbar. Kinetic studies showed that pressure and temperature did not always act synergistically with respect to enzyme inactivation. FTIR-spectroscopy showed that pressure- or temperature-induced changes were considerably different. Both temperature and pressure-temperature inactivation were only slightly influenced by pH (in the pH-range 5.5–7.5).

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